PXD016778

PXD016778 is an original dataset announced via ProteomeXchange.

Title	Semi-Synthesis of an Evasin from Tick Saliva Reveals a Critical Role of Tyrosine Sulfation for Chemokine Binding and Inhibition
Description	Blood feeding arthropods produce anti-inflammatory salivary proteins called evasins that function through inhibition of chemokine-receptor signalling in the host. Herein, we show that the evasin ACA-01 from the Amblyomma cajennense tick can be post-translationally sulfated at two tyrosine residues, albeit as a mixture of sulfated variants. Homogenously sulfated variants of the proteins were efficiently assembled via a semi-synthetic native chemical ligation strategy. Sulfation significantly improved the binding affinity of ACA-01 for a range of pro-inflammatory chemokines and also enhanced the ability of ACA-01 to inhibit chemokine signalling through cognate receptors. Comparisons of evasin sequences and structural data suggest that tyrosine sulfation serves as a receptor mimetic strategy for recognizing and suppressing the pro-inflammatory activity of a wide variety of mammalian chemokines. As such, the use incorporation of this PTM or mimics thereof into evasins may provide a strategy to optimize these salivary tick proteins for anti-inflammatory applications
HostingRepository	PRIDE
AnnounceDate	2020-05-15
AnnouncementXML	Submission_2020-08-11_03:13:30.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Mark Larance
SpeciesList	scientific name: Amblyomma cajennense; NCBI TaxID: 34607;
ModificationList	sulfated residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2019-12-16 08:09:50	ID requested
1	2020-05-14 23:57:26	announced
⏵ 2	2020-08-11 03:13:31	announced	2020-08-11: Updated publication reference for PubMed record(s): 32461364.

Franck C, Foster SR, Johansen-Leete J, Chowdhury S, Cielesh M, Bhusal RP, Mackay JP, Larance M, Stone MJ, Payne RJ, Semisynthesis of an evasin from tick saliva reveals a critical role of tyrosine sulfation for chemokine binding and inhibition. Proc Natl Acad Sci U S A, 117(23):12657-12664(2020) [pubmed]

submitter keyword: Sulfation, Synthetic, Evasin, Chemokine

Mark Larance
contact affiliation	University of Sydney
contact email	mark.larance@sydney.edu.au
lab head
Mark Larance
contact affiliation	The University of Sydney
contact email	mark.larance@sydney.edu.au
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/05/PXD016778

PRIDE project URI

• PRIDE
  1. PXD016778
     1. Label: PRIDE project
     2. Name: Semi-Synthesis of an Evasin from Tick Saliva Reveals a Critical Role of Tyrosine Sulfation for Chemokine Binding and Inhibition